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A3660

Sigma-Aldrich

Apoferritin from equine spleen

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.25

form

glycerol solution (50% glycerol and 0.075 M NaCl)

Quality Level

packaging

vial of 50 mg

storage temp.

−20°C

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Application

Apoferritin is a gel filtration molecular weight marker that can be used in gel filtration chromatography and protein chromatography. Apoferritin has the ability to demetallate hemin and to metallate protoporphyrin IX.

related product

Product No.
Description
Pricing

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Noëlle Carette et al.
Journal of inorganic biochemistry, 100(8), 1426-1435 (2006-06-20)
Earlier crystallographic and spectroscopic studies had shown that horse spleen apoferritin was capable of removing the metal ion from hemin (Fe(III)-protoporphyrin IX) [G. Précigoux, J. Yariv, B. Gallois, A. Dautant, C. Courseille, B. Langlois d'Estaintot, Acta Cryst. D50 (1994) 739-743;
David P Klebl et al.
Acta crystallographica. Section D, Structural biology, 76(Pt 4), 340-349 (2020-04-08)
Despite the great strides made in the field of single-particle cryogenic electron microscopy (cryo-EM) in microscope design, direct electron detectors and new processing suites, the area of sample preparation is still far from ideal. Traditionally, sample preparation involves blotting, which
Xindong Wang et al.
Biosensors & bioelectronics, 47, 171-177 (2013-04-11)
A novel sandwich electrochemical immunoassay was developed for ultrasensitive detection of avian leukosis virus subgroup J (ALVs-J) using graphene quantum dots (GQDs) and apoferritin-encapsulated Cu (Cu-apoferritin) nanoparticles for signal amplification. GQDs were used both for the conjugation of primary ALVs-J
Venkata P Dandey et al.
Journal of structural biology, 202(2), 161-169 (2018-01-26)
We present an update describing new features and applications of Spotiton, a novel instrument for vitrifying samples for cryoEM. We have used Spotiton to prepare several test specimens that can be reconstructed using routine single particle analysis to ∼3 Å resolution
Richard Henderson et al.
Microscopy (Oxford, England), 62(1), 43-50 (2013-01-08)
Theoretical considerations together with simulations of single-particle electron cryomicroscopy images of biological assemblies in ice demonstrate that atomic structures should be obtainable from images of a few thousand asymmetric units, provided the molecular weight of the whole assembly being studied

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